Evidence map›Paper›PMID 28874050›Full record

ArticleMolecular pharmaceutics2017

Thermal Gradient Mid- and Far-Infrared Spectroscopy as Tools for Characterization of Protein Carbohydrate Lyophilizates.

M A Mensink, J Šibík, H W Frijlink, K van der Voort Maarschalk, W L J Hinrichs, J A Zeitler

Open access · hybridAbstract read
In one paragraph

Article in Molecular pharmaceutics, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
2.2field-weighted citation impact, top 12% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

2 citing papers in PubMed, 13 citations in OpenAlex.

  1. Article
  2. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 3 countries.

M A MensinkDepartment of Pharmaceutical Technology and Biopharmacy, University of Groningen , Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands.ORCID 0000-0002-6961-7776
J ŠibíkDepartment of Chemical Engineering and Biotechnology, University of Cambridge , Philippa Fawcett Drive, Cambridge CB3 0AS, United Kingdom.
H W FrijlinkDepartment of Pharmaceutical Technology and Biopharmacy, University of Groningen , Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands.
K van der Voort MaarschalkDepartment of Pharmaceutical Technology and Biopharmacy, University of Groningen , Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands.
W L J HinrichsDepartment of Pharmaceutical Technology and Biopharmacy, University of Groningen , Antonius Deusinglaan 1, 9713 AV Groningen, The Netherlands.
J A ZeitlerDepartment of Chemical Engineering and Biotechnology, University of Cambridge , Philippa Fawcett Drive, Cambridge CB3 0AS, United Kingdom.ORCID 0000-0002-4958-0582
University of Groningen · NLRoche (Switzerland) · CHUniversity of Cambridge · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein drugs play an important role in modern day medicine. Typically, these proteins are formulated as liquids requiring cold chain processing. To circumvent the cold chain and achieve better storage stability, these proteins can be dried in the presence of carbohydrates. We demonstrate that thermal gradient mid- and far-infrared spectroscopy (FTIR and THz-TDS, respectively) can provide useful information about solid-state protein carbohydrate formulations regarding mobility and intermolecular interactions. A model protein (BSA) was lyophilized in the presence of three carbohydrates with different size and protein stabilizing capacity. A gradual increase in mobility was observed with increasing temperature in formulations containing protein and/or larger carbohydrates (oligo- or polysaccharides), lacking a clear onset of fast mobility as was observed for smaller molecules. Furthermore, both techniques are able to identify the glass transition temperatures (T

Indexed as

BiopharmaceuticsCarbohydratesChemistry, PharmaceuticalDrug CompoundingFreeze DryingHydrogen BondingMolecular WeightPharmaceutical PreparationsProteinsProtein StabilitySpectroscopy, Fourier Transform InfraredTemperatureTerahertz SpectroscopyCarbohydratesPharmaceutical PreparationsProteinsFourier transform infrared spectroscopy (FTIR)hydrogen bondingmolecular mobilitysolid stateterahertz time-domain spectroscopy (THz-TDS)

Identifiers

PMID28874050
PMCPMC5627341
OpenAlexW2751528354

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.